BMRB Entry 17714
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17714
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Title: human prion protein mutant HuPrP(90-231, M129, V210I) PubMed: 21839748
Deposition date: 2011-06-16 Original release date: 2011-08-19
Authors: Biljan, Ivana; Ilc, Gregor; Giachin, Gabriele; Raspadori, Andrea; Zhukov, Igor; Plavec, Janez; Legname, Giuseppe
Citation: Biljan, Ivana; Ilc, Gregor; Giachin, Gabriele; Raspadori, Andrea; Zhukov, Igor; Plavec, Janez; Legname, Giuseppe. "Toward the molecular basis of inherited prion diseases: NMR structure of the human prion protein with V210I mutation." J. Mol. Biol. 412, 660-673 (2011).
Assembly members:
HuPrP, polymer, 147 residues, 16654.660 Da.
Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
HuPrP: GAMDPGQGGGTHSQWNKPSK
PKTNMKHMAGAAAAGAVVGG
LGGYMLGSAMSRPIIHFGSD
YEDRYYRENMHRYPNQVYYR
PMDEYSNQNNFVHDCVNITI
KQHTVTTTTKGENFTETDVK
MMERVIEQMCITQYERESQA
YYQRGSS
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 459 |
| 15N chemical shifts | 149 |
| 1H chemical shifts | 928 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | HuPrP | 1 |
Entities:
Entity 1, HuPrP 147 residues - 16654.660 Da.
Gly85-Pro89 nonnative
| 1 | GLY | ALA | MET | ASP | PRO | GLY | GLN | GLY | GLY | GLY | ||||
| 2 | THR | HIS | SER | GLN | TRP | ASN | LYS | PRO | SER | LYS | ||||
| 3 | PRO | LYS | THR | ASN | MET | LYS | HIS | MET | ALA | GLY | ||||
| 4 | ALA | ALA | ALA | ALA | GLY | ALA | VAL | VAL | GLY | GLY | ||||
| 5 | LEU | GLY | GLY | TYR | MET | LEU | GLY | SER | ALA | MET | ||||
| 6 | SER | ARG | PRO | ILE | ILE | HIS | PHE | GLY | SER | ASP | ||||
| 7 | TYR | GLU | ASP | ARG | TYR | TYR | ARG | GLU | ASN | MET | ||||
| 8 | HIS | ARG | TYR | PRO | ASN | GLN | VAL | TYR | TYR | ARG | ||||
| 9 | PRO | MET | ASP | GLU | TYR | SER | ASN | GLN | ASN | ASN | ||||
| 10 | PHE | VAL | HIS | ASP | CYS | VAL | ASN | ILE | THR | ILE | ||||
| 11 | LYS | GLN | HIS | THR | VAL | THR | THR | THR | THR | LYS | ||||
| 12 | GLY | GLU | ASN | PHE | THR | GLU | THR | ASP | VAL | LYS | ||||
| 13 | MET | MET | GLU | ARG | VAL | ILE | GLU | GLN | MET | CYS | ||||
| 14 | ILE | THR | GLN | TYR | GLU | ARG | GLU | SER | GLN | ALA | ||||
| 15 | TYR | TYR | GLN | ARG | GLY | SER | SER |
Samples:
sample_1: HuPrP, [U-100% 13C; U-100% 15N], 0.6 mM; sodium acetate 20 mM; H2O 90%; D2O 10%
sample_2: HuPrP, [U-100% 13C; U-100% 15N], 0.6 mM; sodium acetate 20 mM; D2O 100%
sample_conditions_1: ionic strength: 0.1 M; pH: 5.5; pressure: 1 atm; temperature: 298 K
sample_conditions_2: ionic strength: 0.1 M; pD: 5.9; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aliphatic | sample_2 | isotropic | sample_conditions_2 |
| 2D 1H-13C HSQC aromatic | sample_2 | isotropic | sample_conditions_2 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_2 | isotropic | sample_conditions_2 |
| 3D 1H-13C NOESY aromatic | sample_2 | isotropic | sample_conditions_2 |
| 3D HCCH-TOCSY | sample_2 | isotropic | sample_conditions_2 |
Software:
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
SPARKY v3.115, Goddard - chemical shift assignment, peak picking
CYANA v3.0, Guntert, Mumenthaler and Wuthrich - structure solution
YASARA v11.5.22, (YASARA) - refinement
ProcheckNMR, Laskowski and MacArthur - data analysis
WhatIF, Vriend - data analysis
NMR spectrometers:
- Varian Uniform NMR System 800 MHz
Related Database Links:
| BMRB | 15676 16743 16757 17756 17757 17780 18426 18550 19268 4379 4402 4434 4620 4641 4736 |
| PDB | |
| DBJ | BAA00011 BAF62360 BAG32276 BAG32277 BAG32278 |
| EMBL | CAA58442 CAG46836 CAG46869 |
| GB | AAA19664 AAA60182 AAA68632 AAA68633 AAB59442 |
| REF | NP_000302 NP_001009093 NP_001073590 NP_001073591 NP_001073592 |
| SP | P04156 P40252 P61766 P61767 P61768 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts